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GLYCOBIOLOGY OF MALARIA PARASITE

GLYCOBIOLOGY OF MALARIA PARASITE
疟疾寄生虫的糖生物学
批准号:
6478939
负责人:
D C GOWDA
金额:
$5.36万
依托单位国家:
美国
项目类别:
财政年份:
2000
资助国家:
美国
项目状态:
已结题
起止时间:
2000-07-01 至 2002-06-30

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中文摘要
翻译
RVV-X(93 KDa)和RVV-V(31 KDa),凝血因子X和V 罗素蛇毒的激活糖蛋白是由 同样的毒腺,并能够激活凝血 因子X和因子V。它们都含有N-键 低聚糖,但不同的糖基化。眼镜蛇毒液 粘蛋白是一种高分子量、高度糖基化的蛋白质 由眼镜蛇毒腺大量分泌。它包含的大部分内容 末端带有cc-半乳糖基的0-连接低聚糖 抗原性决定因素。最近的研究表明,这种粘蛋白 激活cc-半乳糖苷残基依赖的人补体 RVV-X、RVV-V和眼镜蛇粘液释放碳水化合物的方式 用电喷雾-质谱仪相结合进行分析, 碰撞诱导分解(CID),对于眼镜蛇粘蛋白,特异的 酶解法。其目标是提供广泛的质量 N-连接葡聚糖的概况和一般结构特征 虽然眼镜蛇粘蛋白低聚体的更具体的结构细节 与抗原性(x-半乳糖)的存在有关 残留物。眼镜蛇粘蛋白中碱释放的低聚糖醛糖醇 在Bio-Gel P30柱上分离,然后用咖啡消化 豆类(x-半乳糖苷酶)。通过比较较小的 酶处理前后的低聚物,结合CID 结构分析表明,(x-半乳糖苷酶敏感性 需要存在末端的己糖-己糖对。这个 内切半乳糖苷酶和CID联合用于探测 内部结构特征,如分支和串联己糖 重复着。完整物种的相对分子质量分布 通过M[Aldi-TOF MS]确定了非常大的低聚物。
英文摘要
RVV-X (93 kDa) and RVV-V (31 kDa), the coagulation factor X and V activating glycoproteins of Russell's Viper venom, are synthesized by the same venom gland and are capable of activating blood coagulation factors X and V, respectively. They both contain N-linked oligosaccharides but are differentially glycosylated. Cobra venom mucin is a high molecular weight, heavily glycosylated protein that is secreted abundantly by the cobra venom gland. It contains largely 0-linked oligosaccharides with terminal cc-galactosylated Le' and Le' antigenic determinants. Recent studies suggest that this mucin activates human complement in an cc-galactoside residue-dependent manner The carbohydrates released from RVV-X., RVV-V and cobra mucin were analyzed by a combination of electrospray mass spectrometry, collision-induced decomposition (CID), and for cobra mucin, specific enzymatic hydrolysis. The objective was to provide broad mass profiles and general structural features for the N-linked glycans while more specific structural details for the cobra mucin oligomers were sought, related to the presence of theantigenic (x-galactose residues. Base-released oligosaccharide alditols from cobra mucins were partitioned on Bio-Gel P 30 columns and then digested with coffee bean (x-galactosidase. By comparing the mass profiles for the smaller oligomers before and after enzyme treatment, combined with CID structural analysis, it was shown that (x-galactosidase sensitivity required the presence of a terminal hexose-hexose pair. The combination of endo-o-galactosidase and CID wasused to probe for internal structural features such as branching and tandem hexose repeats. Molecular weight distributions of the intact species of the very large oligomers are being determined by M[ALDI-TOF MS.
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